PLPP6_BOVIN
ID PLPP6_BOVIN Reviewed; 289 AA.
AC Q58DI5; A6QLK7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q8IY26};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q8IY26};
DE EC=3.6.1.68 {ECO:0000250|UniProtKB:Q8IY26};
DE AltName: Full=Phospholipid phosphatase 6 {ECO:0000250|UniProtKB:Q8IY26};
GN Name=PLPP6 {ECO:0000250|UniProtKB:Q8IY26};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Magnesium-independent polyisoprenoid diphosphatase that
CC catalyzes the sequential dephosphorylation of presqualene, farnesyl,
CC geranyl and geranylgeranyl diphosphates. Functions in the innate immune
CC response through the dephosphorylation of presqualene diphosphate which
CC acts as a potent inhibitor of the signaling pathways contributing to
CC polymorphonuclear neutrophils activation. May regulate the biosynthesis
CC of cholesterol and related sterols by dephosphorylating presqualene and
CC farnesyl diphosphate, two key intermediates in this biosynthetic
CC pathway. May also play a role in protein prenylation by acting on
CC farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two
CC precursors for the addition of isoprenoid anchors to membrane proteins.
CC Has a lower activity towards phosphatidic acid (PA), but through
CC phosphatidic acid dephosphorylation may participate in the biosynthesis
CC of phospholipids and triacylglycerols. May also act on ceramide-1-P,
CC lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-
CC 1-phosphate. {ECO:0000250|UniProtKB:Q8IY26}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + presqualene diphosphate = H(+) + phosphate + presqualene
CC monophosphate; Xref=Rhea:RHEA:67968, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57310,
CC ChEBI:CHEBI:176803; Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67969;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + presqualene monophosphate = phosphate + presqualene
CC alcohol; Xref=Rhea:RHEA:68024, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:176803, ChEBI:CHEBI:176962;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68025;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesyl
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:48128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:88226, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48129;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl phosphate + H2O = (2E,6E)-farnesol +
CC phosphate; Xref=Rhea:RHEA:48132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:43474, ChEBI:CHEBI:88226;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48133;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (2E,6E,10E)-
CC geranylgeranyl phosphate + H(+) + phosphate; Xref=Rhea:RHEA:68008,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:144936;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68009;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl phosphate + H2O = (2E,6E,10E)-
CC geranylgeraniol + phosphate; Xref=Rhea:RHEA:68016, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46762, ChEBI:CHEBI:144936;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68017;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+)
CC + phosphate; Xref=Rhea:RHEA:47944, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:88107; EC=3.6.1.68;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47945;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl phosphate + H2O = (2E)-geraniol + phosphate;
CC Xref=Rhea:RHEA:68020, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:88107;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68021;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:Q8IY26};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8IY26}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8IY26}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q8IY26}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q8IY26}.
CC -!- PTM: Phosphorylation by PKC activates the phosphatase activity towards
CC presqualene diphosphate. {ECO:0000250|UniProtKB:Q8IY26}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; BT021612; AAX46459.1; -; mRNA.
DR EMBL; BC147999; AAI48000.1; -; mRNA.
DR RefSeq; NP_001019744.1; NM_001024573.1.
DR AlphaFoldDB; Q58DI5; -.
DR SMR; Q58DI5; -.
DR STRING; 9913.ENSBTAP00000014674; -.
DR PaxDb; Q58DI5; -.
DR Ensembl; ENSBTAT00000014674; ENSBTAP00000014674; ENSBTAG00000011050.
DR GeneID; 541021; -.
DR KEGG; bta:541021; -.
DR CTD; 403313; -.
DR VEuPathDB; HostDB:ENSBTAG00000011050; -.
DR VGNC; VGNC:33049; PLPP6.
DR eggNOG; KOG4268; Eukaryota.
DR GeneTree; ENSGT00940000156166; -.
DR HOGENOM; CLU_072573_4_0_1; -.
DR InParanoid; Q58DI5; -.
DR OMA; GVCAGEN; -.
DR OrthoDB; 1356295at2759; -.
DR TreeFam; TF323272; -.
DR Reactome; R-BTA-191273; Cholesterol biosynthesis.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000011050; Expressed in oviduct epithelium and 107 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0045339; P:farnesyl diphosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0033383; P:geranyl diphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:1902247; P:geranylgeranyl diphosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006720; P:isoprenoid metabolic process; ISS:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:1902565; P:positive regulation of neutrophil activation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; ISS:UniProtKB.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Immunity; Innate immunity;
KW Lipid metabolism; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Polyisoprenoid diphosphate/phosphate
FT phosphohydrolase PLPP6"
FT /id="PRO_0000239395"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..158
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..254
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..186
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 205..208
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 243..254
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 208
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 254
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY26"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D4F2"
SQ SEQUENCE 289 AA; 31886 MW; 29D4F6227B4D3767 CRC64;
MQSPRRNAEG RPLGTCDPSS SGSPAHGGGS RFEFQSLLSS RMPGADPTSA RLRASESPVH
RRGSFPLAGA GSSQALPPQL PEEDRIDLNP SFLGIALRSL LAIDLWLSKK LGVCAGESSS
WGSMRPLMKL LEISGHGIPW LLGTLYCLSR SDSWAGREVL MNLLFALLLD LLLVSLIKGL
VRRRRPAHNQ MDMFFTISVD KYSFPSGHTT RAALVSRFIL NHLVLAIPLR VLVVLWAFIL
GLSRVMLGRH NVTDVAFGFF LGYMQYSIVD YCWLSPRTAP VLFVLWNQP
